Published April 2019
| Accepted Version
Journal Article
Open
Selective C-H bond functionalization with engineered heme proteins: new tools to generate complexity
Abstract
C-H functionalization is an attractive strategy to construct and diversify molecules. Heme proteins, predominantly cytochromes P450, are responsible for an array of C-H oxidations in biology. Recent work has coupled concepts from synthetic chemistry, computation, and natural product biosynthesis to engineer heme protein systems to deliver products with tailored oxidation patterns. Heme protein catalysis has been shown to go well beyond these native reactions and now accesses new-to-nature C-H transformations, including C-N and C-C bond forming processes. Emerging work with these systems moves us along the ambitious path of building complexity from the ubiquitous C-H bond.
Additional Information
© 2018 Elsevier. Available online 18 October 2018. This work was supported by the NSF, Division of Molecular and Cellular Biosciences (grant MCB-1513007). R. K. Z. acknowledges support from the NSF Graduate Research Fellowship (grant DGE-1144469) and the Donna and Benjamin M. Rosen Bioengineering Center. X. H. is supported by an NIH pathway to independence award (grant K99GM129419). Conflict of interest statement: Nothing declared.Attached Files
Accepted Version - nihms-1510154.pdf
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nihms-1510154.pdf
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Additional details
- PMCID
- PMC6461521
- Eprint ID
- 90453
- Resolver ID
- CaltechAUTHORS:20181029-094838266
- Donna and Benjamin M. Rosen Bioengineering Center
- NSF
- MCB-1513007
- NSF Graduate Research Fellowship
- DGE-1144469
- NIH
- K99GM129419
- Created
-
2018-10-29Created from EPrint's datestamp field
- Updated
-
2022-02-15Created from EPrint's last_modified field
- Caltech groups
- Rosen Bioengineering Center